Dependency on serine concentration of the activity of tryptophan synthase. Cooperative properties.
The activity of the enzyme tryptophan synthase from Escherichia coli was tested as a function of the concentration of L-serine which serves as a substrate in the indole to tryptophan reaction as well as for the L-serine deaminase activity. L-Serine binding was found to follow the pattern of negative cooperativity both by kinetic and by equilibrium methods. The enzyme kinetic data support the view that a rapid equilibration model for the enzyme . substrates complex formation is not strictly obeyed.
D004926:Escherichia coli / Q000201:enzymology; D007211:Indoles / Q000378:metabolism; D007700:Kinetics; D011485:Protein Binding; D012694:Serine / Q000378:metabolism*; D014364:Tryptophan / Q000378:metabolism; D014367:Tryptophan Synthase / Q000378:metabolism*; D014462:Ultrafiltration
D007211:Indoles; D012694:Serine; C030374:indole; D014364:Tryptophan; D014367:Tryptophan Synthase